Q4QI30 · Q4QI30_LEIMA
- ProteinEndonuclease III homolog
- GeneNTH1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids257 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base excision repair (BER), the primary repair pathway for the repair of oxidative DNA damage. The DNA N-glycosylase activity releases the damaged DNA base from DNA by cleaving the N-glycosidic bond, leaving an AP site. The AP lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination. Primarily recognizes and repairs oxidative base damage of pyrimidines.
Catalytic activity
- 2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-phospho-2'-deoxyribonucleoside-DNA + H+
Cofactor
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrion | |
Cellular Component | nucleus | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | class I DNA-(apurinic or apyrimidinic site) endonuclease activity | |
Molecular Function | DNA binding | |
Molecular Function | DNA-(apurinic or apyrimidinic site) endonuclease activity | |
Molecular Function | endonuclease activity | |
Molecular Function | metal ion binding | |
Molecular Function | oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity | |
Biological Process | base-excision repair, AP site formation | |
Biological Process | nucleotide-excision repair |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameEndonuclease III homolog
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Discoba > Euglenozoa > Kinetoplastea > Metakinetoplastina > Trypanosomatida > Trypanosomatidae > Leishmaniinae > Leishmania
Accessions
- Primary accessionQ4QI30
Proteomes
Organism-specific databases
Subcellular Location
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 58-208 | HhH-GPD | ||||
Sequence: LSAQTKDVVTAAAMDTLIKRELTVQSVHAMTETELDKHICKVGFHNTKARNIKEVAAILMKNYDGKVPREYAELIALPGVGPKMANLFFQDADHRVIGIGVDTHVHRISQRYRWVPSTVKTPEDTRKALESWLPREHWGTINSLMVGLGQT | ||||||
Region | 237-257 | Disordered | ||||
Sequence: RLRAKAPLMEKEEPVSHRKRR |
Sequence similarities
Belongs to the Nth/MutY family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length257
- Mass (Da)29,495
- Last updated2005-07-19 v1
- ChecksumACFBF8754A67EB2D
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
FR796405 EMBL· GenBank· DDBJ | CAJ02303.1 EMBL· GenBank· DDBJ | Genomic DNA |